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Protein

Atrial natriuretic peptide receptor 2

Gene

NPR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth.5 Publications

Catalytic activityi

GTP = 3',5'-cyclic GMP + diphosphate.1 Publication

GO - Molecular functioni

  • ATP binding Source: Ensembl
  • GTP binding Source: UniProtKB-KW
  • guanylate cyclase activity Source: UniProtKB
  • hormone binding Source: UniProtKB
  • natriuretic peptide receptor activity Source: UniProtKB
  • peptide hormone binding Source: UniProtKB
  • protein kinase activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Receptor

Keywords - Biological processi

cGMP biosynthesis, Osteogenesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS08430-MONOMER.
BRENDAi4.6.1.2. 2681.
ReactomeiR-HSA-5578768. Physiological factors.

Protein family/group databases

TCDBi8.A.85.1.2. the guanylate cyclase (gc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Atrial natriuretic peptide receptor 2 (EC:4.6.1.21 Publication)
Alternative name(s):
Atrial natriuretic peptide receptor type B
Short name:
ANP-B
Short name:
ANPR-B
Short name:
NPR-B
Guanylate cyclase B
Short name:
GC-B
Gene namesi
Name:NPR2
Synonyms:ANPRB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:7944. NPR2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini23 – 458ExtracellularSequence analysisAdd BLAST436
Transmembranei459 – 478HelicalSequence analysisAdd BLAST20
Topological domaini479 – 1047CytoplasmicSequence analysisAdd BLAST569

GO - Cellular componenti

  • guanylate cyclase complex, soluble Source: GO_Central
  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Acromesomelic dysplasia, Maroteaux type (AMDM)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive acromesomelic chondrodysplasia. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMDM is characterized by axial skeletal involvement with wedging of vertebral bodies. In AMDM all skeletal elements are present but show abnormal rates of linear growth.
See also OMIM:602875
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02258332P → T in AMDM. 1 PublicationCorresponds to variant rs28931581dbSNPEnsembl.1
Natural variantiVAR_022584115W → G in AMDM; markedly deficient activity. 1 PublicationCorresponds to variant rs28931582dbSNPEnsembl.1
Natural variantiVAR_022585176D → E in AMDM. 1 PublicationCorresponds to variant rs28929479dbSNPEnsembl.1
Natural variantiVAR_022586297T → M in AMDM; markedly deficient activity. 1 Publication1
Natural variantiVAR_022587338Y → C in AMDM. 1 Publication1
Natural variantiVAR_022588409A → T in AMDM. 1 Publication1
Natural variantiVAR_022589413G → E in AMDM; markedly deficient activity. 1 Publication1
Natural variantiVAR_076481658L → F in AMDM; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity; loss of natriuretic peptide receptor activity; dominant negative effect. 2 Publications1
Natural variantiVAR_022590708Y → C in AMDM; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity. 2 Publications1
Natural variantiVAR_022591776R → W in AMDM; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity. 2 Publications1
Natural variantiVAR_022592957R → C in AMDM. 1 PublicationCorresponds to variant rs370158184dbSNPEnsembl.1
Natural variantiVAR_022593959G → A in AMDM; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity. 2 Publications1
Epiphyseal chondrodysplasia, Miura type (ECDM)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn overgrowth syndrome characterized by tall stature, long hands and feet with arachnodactyly, macrodactyly of the great toes, scoliosis, coxa valga and slipped capital femoral epiphysis.
See also OMIM:615923
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071875488A → P in ECDM; mutant and wild-type alleles have similar expression levels; the mutation results in increased guanylate cyclase activity. 1 PublicationCorresponds to variant rs587777597dbSNPEnsembl.1
Natural variantiVAR_071876655R → C in ECDM; the mutation results in increased guanylate cyclase activity. 1 PublicationCorresponds to variant rs587777596dbSNPEnsembl.1
Natural variantiVAR_071877882V → M in ECDM; the mutation results in higher guanylate cyclase activity; causes a 15-fold increase in basal Vmax; has higher affinity for GTP than wild-type in the presence of NPPC; might lead to a structural change that locks the enzyme in a conformation mimicking the ATP-bound state. 2 Publications1
Short stature with non-specific skeletal abnormalities (SNSK)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition characterized by short stature, defined as a height less than 2 SD below normal, and no endocrine abnormalities.
See also OMIM:616255
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07467876S → P in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; loss of localization to the plasma membrane. 1 PublicationCorresponds to variant rs796065355dbSNPEnsembl.1
Natural variantiVAR_074679110R → C in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; retained in the endoplasmic reticulum. 1 PublicationCorresponds to variant rs758478717dbSNPEnsembl.1
Natural variantiVAR_074681263R → P in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; loss of localization to the plasma membrane. 1 Publication1
Natural variantiVAR_074682417Q → E in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; no effect on cell surface expression. 1 PublicationCorresponds to variant rs796065356dbSNPEnsembl.1
Natural variantiVAR_074683819R → C in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; no effect on cell surface expression. 1 PublicationCorresponds to variant rs766256429dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi24N → D or Q: Decreased glycosylation. Decreased guanylate cyclase activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi4882.
MalaCardsiNPR2.
MIMi602875. phenotype.
615923. phenotype.
616255. phenotype.
OpenTargetsiENSG00000159899.
Orphaneti40. Acromesomelic dysplasia, Maroteaux type.
329191. Tall stature - scoliosis - macrodactyly of the great toes.
PharmGKBiPA257.

Chemistry databases

ChEMBLiCHEMBL2111337.
DrugBankiDB01613. Erythrityl Tetranitrate.
DB04899. Nesiritide.
GuidetoPHARMACOLOGYi1748.

Polymorphism and mutation databases

BioMutaiNPR2.
DMDMi113916.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000001236423 – 1047Atrial natriuretic peptide receptor 2Add BLAST1025

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi24N-linked (GlcNAc...)Sequence analysis1
Glycosylationi35N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi75 ↔ 101By similarity
Glycosylationi161N-linked (GlcNAc...)Sequence analysis1
Glycosylationi195N-linked (GlcNAc...)Sequence analysis1
Glycosylationi244N-linked (GlcNAc...)Sequence analysis1
Glycosylationi277N-linked (GlcNAc...)Sequence analysis1
Glycosylationi349N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi439InterchainCurated
Disulfide bondi448InterchainCurated
Modified residuei513Phosphoserine1 Publication1
Modified residuei516Phosphothreonine1 Publication1
Modified residuei518Phosphoserine1 Publication1
Modified residuei522PhosphoserineBy similarity1
Modified residuei523Phosphoserine1 Publication1
Modified residuei526Phosphoserine1 Publication1
Modified residuei529Phosphothreonine1 Publication1

Post-translational modificationi

Phosphorylated (PubMed:26980729). Phosphorylation of the protein kinase-like domain is required for full activation by CNP (By similarity).By similarity1 Publication
Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP20594.
MaxQBiP20594.
PaxDbiP20594.
PeptideAtlasiP20594.
PRIDEiP20594.

PTM databases

iPTMnetiP20594.
PhosphoSitePlusiP20594.

Expressioni

Gene expression databases

BgeeiENSG00000159899.
CleanExiHS_NPR2.
ExpressionAtlasiP20594. baseline and differential.
GenevisibleiP20594. HS.

Organism-specific databases

HPAiHPA011977.

Interactioni

Protein-protein interaction databases

BioGridi110942. 4 interactors.
IntActiP20594. 2 interactors.
STRINGi9606.ENSP00000341083.

Structurei

3D structure databases

ProteinModelPortaliP20594.
SMRiP20594.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini513 – 786Protein kinasePROSITE-ProRule annotationAdd BLAST274
Domaini861 – 991Guanylate cyclasePROSITE-ProRule annotationAdd BLAST131

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
Contains 1 guanylate cyclase domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1023. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000118959.
HOVERGENiHBG051862.
InParanoidiP20594.
KOiK12324.
OMAiHQVYTRE.
OrthoDBiEOG091G02QS.
PhylomeDBiP20594.
TreeFamiTF106338.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR001170. ANPR/GUC.
IPR011009. Kinase-like_dom.
IPR029787. Nucleotide_cyclase.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00255. NATPEPTIDER.
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00458. ANF_RECEPTORS. 1 hit.
PS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P20594-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MALPSLLLLV AALAGGVRPP GARNLTLAVV LPEHNLSYAW AWPRVGPAVA
60 70 80 90 100
LAVEALGRAL PVDLRFVSSE LEGACSEYLA PLSAVDLKLY HDPDLLLGPG
110 120 130 140 150
CVYPAASVAR FASHWRLPLL TAGAVASGFS AKNDHYRTLV RTGPSAPKLG
160 170 180 190 200
EFVVTLHGHF NWTARAALLY LDARTDDRPH YFTIEGVFEA LQGSNLSVQH
210 220 230 240 250
QVYAREPGGP EQATHFIRAN GRIVYICGPL EMLHEILLQA QRENLTNGDY
260 270 280 290 300
VFFYLDVFGE SLRAGPTRAT GRPWQDNRTR EQAQALREAF QTVLVITYRE
310 320 330 340 350
PPNPEYQEFQ NRLLIRARED FGVELGPSLM NLIAGCFYDG ILLYAEVLNE
360 370 380 390 400
TIQEGGTRED GLRIVEKMQG RRYHGVTGLV VMDKNNDRET DFVLWAMGDL
410 420 430 440 450
DSGDFQPAAH YSGAEKQIWW TGRPIPWVKG APPSDNPPCA FDLDDPSCDK
460 470 480 490 500
TPLSTLAIVA LGTGITFIMF GVSSFLIFRK LMLEKELASM LWRIRWEELQ
510 520 530 540 550
FGNSERYHKG AGSRLTLSLR GSSYGSLMTA HGKYQIFANT GHFKGNVVAI
560 570 580 590 600
KHVNKKRIEL TRQVLFELKH MRDVQFNHLT RFIGACIDPP NICIVTEYCP
610 620 630 640 650
RGSLQDILEN DSINLDWMFR YSLINDLVKG MAFLHNSIIS SHGSLKSSNC
660 670 680 690 700
VVDSRFVLKI TDYGLASFRS TAEPDDSHAL YAKKLWTAPE LLSGNPLPTT
710 720 730 740 750
GMQKADVYSF GIILQEIALR SGPFYLEGLD LSPKEIVQKV RNGQRPYFRP
760 770 780 790 800
SIDRTQLNEE LVLLMERCWA QDPAERPDFG QIKGFIRRFN KEGGTSILDN
810 820 830 840 850
LLLRMEQYAN NLEKLVEERT QAYLEEKRKA EALLYQILPH SVAEQLKRGE
860 870 880 890 900
TVQAEAFDSV TIYFSDIVGF TALSAESTPM QVVTLLNDLY TCFDAIIDNF
910 920 930 940 950
DVYKVETIGD AYMVVSGLPG RNGQRHAPEI ARMALALLDA VSSFRIRHRP
960 970 980 990 1000
HDQLRLRIGV HTGPVCAGVV GLKMPRYCLF GDTVNTASRM ESNGQALKIH
1010 1020 1030 1040
VSSTTKDALD ELGCFQLELR GDVEMKGKGK MRTYWLLGER KGPPGLL
Length:1,047
Mass (Da):117,022
Last modified:February 1, 1991 - v1
Checksum:i817FB74D6B31F7EF
GO
Isoform Short (identifier: P20594-2) [UniParc]FASTAAdd to basket
Also known as: NPR-BI

The sequence of this isoform differs from the canonical sequence as follows:
     964-1047: PVCAGVVGLK...GERKGPPGLL → KADSHSSPSLHLSQTLPTCFFSKGQSVLGLLA

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:995
Mass (Da):111,208
Checksum:i745D41E451E0D7DF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti755T → S in BAA81737 (PubMed:10082481).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02258332P → T in AMDM. 1 PublicationCorresponds to variant rs28931581dbSNPEnsembl.1
Natural variantiVAR_07467876S → P in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; loss of localization to the plasma membrane. 1 PublicationCorresponds to variant rs796065355dbSNPEnsembl.1
Natural variantiVAR_074679110R → C in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; retained in the endoplasmic reticulum. 1 PublicationCorresponds to variant rs758478717dbSNPEnsembl.1
Natural variantiVAR_022584115W → G in AMDM; markedly deficient activity. 1 PublicationCorresponds to variant rs28931582dbSNPEnsembl.1
Natural variantiVAR_022585176D → E in AMDM. 1 PublicationCorresponds to variant rs28929479dbSNPEnsembl.1
Natural variantiVAR_074680187V → I Rare polymorphism; does not affect C-type natriuretic peptide-induced signaling. 1 PublicationCorresponds to variant rs768423636dbSNPEnsembl.1
Natural variantiVAR_042219232M → I.1 PublicationCorresponds to variant rs55747238dbSNPEnsembl.1
Natural variantiVAR_074681263R → P in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; loss of localization to the plasma membrane. 1 Publication1
Natural variantiVAR_022586297T → M in AMDM; markedly deficient activity. 1 Publication1
Natural variantiVAR_022587338Y → C in AMDM. 1 Publication1
Natural variantiVAR_022588409A → T in AMDM. 1 Publication1
Natural variantiVAR_022589413G → E in AMDM; markedly deficient activity. 1 Publication1
Natural variantiVAR_074682417Q → E in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; no effect on cell surface expression. 1 PublicationCorresponds to variant rs796065356dbSNPEnsembl.1
Natural variantiVAR_071875488A → P in ECDM; mutant and wild-type alleles have similar expression levels; the mutation results in increased guanylate cyclase activity. 1 PublicationCorresponds to variant rs587777597dbSNPEnsembl.1
Natural variantiVAR_071876655R → C in ECDM; the mutation results in increased guanylate cyclase activity. 1 PublicationCorresponds to variant rs587777596dbSNPEnsembl.1
Natural variantiVAR_076481658L → F in AMDM; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity; loss of natriuretic peptide receptor activity; dominant negative effect. 2 Publications1
Natural variantiVAR_022590708Y → C in AMDM; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity. 2 Publications1
Natural variantiVAR_011968771Q → E.Corresponds to variant rs5816dbSNPEnsembl.1
Natural variantiVAR_022591776R → W in AMDM; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity. 2 Publications1
Natural variantiVAR_074683819R → C in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; no effect on cell surface expression. 1 PublicationCorresponds to variant rs766256429dbSNPEnsembl.1
Natural variantiVAR_042220882V → I.1 PublicationCorresponds to variant rs55700371dbSNPEnsembl.1
Natural variantiVAR_071877882V → M in ECDM; the mutation results in higher guanylate cyclase activity; causes a 15-fold increase in basal Vmax; has higher affinity for GTP than wild-type in the presence of NPPC; might lead to a structural change that locks the enzyme in a conformation mimicking the ATP-bound state. 2 Publications1
Natural variantiVAR_022592957R → C in AMDM. 1 PublicationCorresponds to variant rs370158184dbSNPEnsembl.1
Natural variantiVAR_022593959G → A in AMDM; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity. 2 Publications1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001810964 – 1047PVCAG…PPGLL → KADSHSSPSLHLSQTLPTCF FSKGQSVLGLLA in isoform Short. 1 PublicationAdd BLAST84

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005647 Genomic DNA. Translation: BAA81737.1.
AJ005282 mRNA. Translation: CAA06466.1.
AL133410 Genomic DNA. Translation: CAI10987.1.
EU326311 Genomic DNA. Translation: ACA05920.1.
EU326311 Genomic DNA. Translation: ACA05921.1.
CH471071 Genomic DNA. Translation: EAW58338.1.
CH471071 Genomic DNA. Translation: EAW58337.1.
CH471071 Genomic DNA. Translation: EAW58339.1.
CH471071 Genomic DNA. Translation: EAW58340.1.
BC023017 mRNA. Translation: AAH23017.1.
CCDSiCCDS6590.1. [P20594-1]
PIRiS05514. OYHUBR.
RefSeqiNP_003986.2. NM_003995.3. [P20594-1]
UniGeneiHs.78518.

Genome annotation databases

EnsembliENST00000342694; ENSP00000341083; ENSG00000159899. [P20594-1]
GeneIDi4882.
KEGGihsa:4882.
UCSCiuc003zyd.4. human. [P20594-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005647 Genomic DNA. Translation: BAA81737.1.
AJ005282 mRNA. Translation: CAA06466.1.
AL133410 Genomic DNA. Translation: CAI10987.1.
EU326311 Genomic DNA. Translation: ACA05920.1.
EU326311 Genomic DNA. Translation: ACA05921.1.
CH471071 Genomic DNA. Translation: EAW58338.1.
CH471071 Genomic DNA. Translation: EAW58337.1.
CH471071 Genomic DNA. Translation: EAW58339.1.
CH471071 Genomic DNA. Translation: EAW58340.1.
BC023017 mRNA. Translation: AAH23017.1.
CCDSiCCDS6590.1. [P20594-1]
PIRiS05514. OYHUBR.
RefSeqiNP_003986.2. NM_003995.3. [P20594-1]
UniGeneiHs.78518.

3D structure databases

ProteinModelPortaliP20594.
SMRiP20594.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110942. 4 interactors.
IntActiP20594. 2 interactors.
STRINGi9606.ENSP00000341083.

Chemistry databases

ChEMBLiCHEMBL2111337.
DrugBankiDB01613. Erythrityl Tetranitrate.
DB04899. Nesiritide.
GuidetoPHARMACOLOGYi1748.

Protein family/group databases

TCDBi8.A.85.1.2. the guanylate cyclase (gc) family.

PTM databases

iPTMnetiP20594.
PhosphoSitePlusiP20594.

Polymorphism and mutation databases

BioMutaiNPR2.
DMDMi113916.

Proteomic databases

EPDiP20594.
MaxQBiP20594.
PaxDbiP20594.
PeptideAtlasiP20594.
PRIDEiP20594.

Protocols and materials databases

DNASUi4882.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342694; ENSP00000341083; ENSG00000159899. [P20594-1]
GeneIDi4882.
KEGGihsa:4882.
UCSCiuc003zyd.4. human. [P20594-1]

Organism-specific databases

CTDi4882.
DisGeNETi4882.
GeneCardsiNPR2.
H-InvDBHIX0034787.
HGNCiHGNC:7944. NPR2.
HPAiHPA011977.
MalaCardsiNPR2.
MIMi108961. gene.
602875. phenotype.
615923. phenotype.
616255. phenotype.
neXtProtiNX_P20594.
OpenTargetsiENSG00000159899.
Orphaneti40. Acromesomelic dysplasia, Maroteaux type.
329191. Tall stature - scoliosis - macrodactyly of the great toes.
PharmGKBiPA257.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1023. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000118959.
HOVERGENiHBG051862.
InParanoidiP20594.
KOiK12324.
OMAiHQVYTRE.
OrthoDBiEOG091G02QS.
PhylomeDBiP20594.
TreeFamiTF106338.

Enzyme and pathway databases

BioCyciZFISH:HS08430-MONOMER.
BRENDAi4.6.1.2. 2681.
ReactomeiR-HSA-5578768. Physiological factors.

Miscellaneous databases

ChiTaRSiNPR2. human.
GeneWikiiNPR2.
GenomeRNAii4882.
PROiP20594.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000159899.
CleanExiHS_NPR2.
ExpressionAtlasiP20594. baseline and differential.
GenevisibleiP20594. HS.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR001170. ANPR/GUC.
IPR011009. Kinase-like_dom.
IPR029787. Nucleotide_cyclase.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00255. NATPEPTIDER.
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00458. ANF_RECEPTORS. 1 hit.
PS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANPRB_HUMAN
AccessioniPrimary (citable) accession number: P20594
Secondary accession number(s): B0ZBF2
, B0ZBF3, D3DRP3, D3DRP4, O60871, Q4VAK7, Q5TCV2, Q8TA93, Q9UQ50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 30, 2016
This is version 189 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.